6CGV

Revised crystal structure of human adenovirus

「4CWU」から置き換えられました 「1VSZ」から置き換えられました

6CGV の概要

• エントリーDOI: 10.2210/pdb6cgv/pdb
• 関連するPDBエントリー: 6b1t
• 分子名称: Hexon protein, Penton protein, Pre-hexon-linking protein IIIa, ... (6 entities in total)
• 機能のキーワード: human adenovirus crystal structure ad5f35 ad35f, virus
• 由来する生物種: Human adenovirus C serotype 5 (HAdV-5); 詳細
• タンパク質・核酸の鎖数: 21
• 化学式量合計: 1532273.95

構造登録者

Natchiar, S.K.,Venkataraman, S.,Nemerow, G.R.,Reddy, V.S. (登録日: 2018-02-21, 公開日: 2018-04-25, 最終更新日: 2024-10-30)

主引用文献

Kundhavai Natchiar, S.,Venkataraman, S.,Mullen, T.M.,Nemerow, G.R.,Reddy, V.S.
Revised Crystal Structure of Human Adenovirus Reveals the Limits on Protein IX Quasi-Equivalence and on Analyzing Large Macromolecular Complexes.
J. Mol. Biol., 430:4132-4141, 2018

PubMed Abstract: We report the revised crystal structure of a pseudo-typed human adenovirus at 3.8-Å resolution that is consistent with the atomic models of minor proteins determined by cryo-electron microscopy. The diffraction data from multiple crystals were rescaled and merged to increase the data completeness. The densities for the minor proteins were initially identified in the phase-refined omit maps that were further improved by the phases from docked poly-alanine models to build atomic structures. While the trimeric fiber molecules are disordered due to flexibility and imposition of 5-fold symmetry, the remaining major capsid proteins hexon and penton base are clearly ordered, with the exception of hypervariable region 1 of hexons, the RGD containing loop, and the N-termini of the penton base. The exterior minor protein IX together with the interior minor proteins IIIa and VIII stabilizes the adenovirus virion. A segment of N-terminal pro-peptide of VI is found in the interior cavities of peripentonal hexons, and the rest of VI is disordered. While the triskelion substructures formed by the N-termini of IX conform to excellent quasi 3-fold symmetry, the tetrameric coiled-coils formed by the C-termini and organized in parallel and anti-parallel arrangement do not exhibit any quasi-symmetry. This observation also conveys the pitfalls of using the quasi-equivalence as validation criteria for the structural analysis of extended (non-modular) capsid proteins such as IX. Together, these results remedy certain discrepancies in the previous X-ray model in agreement with the cryo-electron microscopy models.

PubMed: 30121295
DOI: 10.1016/j.jmb.2018.08.011

実験手法

X-RAY DIFFRACTION (3.8 Å)